Abstract
Wheat germ albumin (WGA) is rich in nutrients and contains a number of antioxidant polypeptides. The effects of microwave-assisted alkaline protease, neutral protease, papain and compound protease on the degree of hydrolysis of WGA and the clearance rate of DPPH• were comparatively studied. The results showed that papain had the best proteolytic activity. The functional properties of WGA and its hydrolysis polypeptides were determined. The results showed that the solubility of WGA increased after papain hydrolysis, and the apparent viscosity and foam stability reduced. Compared with the amino acids of WGA, the proportions of proline, histidine, glycine, lysine, and glutamic acid in the enzymatic hydrolysis products increased, while the proportions of leucine, phenylalanine, arginine and isoleucine decreased. After papain hydrolysis, the surface structure was loose, and the surrounding blocks became more rounded.
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